7kc4

Human WLS in complex with WNT8A

Method: ELECTRON MICROSCOPY Dmax: 113.3 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Protein Wnt-8a

Homo sapiens

UniProt Q9H1J5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–351 Not recorded Protein wntless homolog × 1 (Q5T9L3) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 PLM PALMITIC ACID × 1 DR9 1-CIS-9-OCTADECANOYL-2-CIS-9-HEXADECANOYL PHOSPHATIDYL GLYCEROL × 3 Y01 CHOLESTEROL HEMISUCCINATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.19 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name WNT8A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 1–351; UniProt 1–351

Protein wntless homolog

Homo sapiens

UniProt Q5T9L3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–541 Not recorded Protein Wnt-8a × 1 (Q9H1J5) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 PLM PALMITIC ACID × 1 DR9 1-CIS-9-OCTADECANOYL-2-CIS-9-HEXADECANOYL PHOSPHATIDYL GLYCEROL × 3 Y01 CHOLESTEROL HEMISUCCINATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.19 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WLS_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–541; UniProt 1–541

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 7kc4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7kc4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7kc4
Deposition date deposition_date2020-10-05
Structure title titleHuman WLS in complex with WNT8A
Keywords keywordsG-protein coupled receptor, palmitoleation, secretion, embryonic development, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier34.11
Radius of gyration Rg (electron density) rg_electron33.70
Forward intensity I(0) i0120211000.00
Molecular weight molecular_weight92389.0 kDa
Excluded volume excluded_volume117510 ų
Envelope volume envelope_volume151760 ų
Hydration-shell volume shell_volume38613 ų
Envelope diameter envelope_diameter120.5
Shell Rg shell_rg38.92
Envelope Rg envelope_rg34.05
Shape Rg shape_rg33.66
Total Rg total_rg34.25
Total atoms total_atoms6477
Residues n_residues771
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax113.3
Rg (real space) rg_real34.31
Rg uncertainty (real space) rg_real_error1.12
I(0) (real space) i0_real1.2020e+08
I(0) uncertainty (real space) i0_real_error2.0230e+06
Rg (reciprocal space) rg_reciprocal34.19
I(0) (reciprocal space) i0_reciprocal120200000.0000
Solution quality estimate total_estimate0.8504
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.5
Skewness Skewness skewness0.505
Kurtosis Kurtosis kurtosis-0.314
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17880000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.590

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)